2j5i: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2j5i.gif|left|200px]]
{{Seed}}
[[Image:2j5i.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2j5i|  PDB=2j5i  |  SCENE=  }}  
{{STRUCTURE_2j5i|  PDB=2j5i  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASE'''
===CRYSTAL STRUCTURE OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASE===




==Overview==
<!--  
The crystal structure of hydroxycinnamoyl-CoA hydratase-lyase (HCHL) from Pseudomonas fluorescens AN103 has been solved to 1.8 A resolution. HCHL is a member of the crotonase superfamily and catalyses the hydration of the acyl-CoA thioester of ferulic acid [3-(4-hydroxy-3-methoxy-phenyl)prop-2-enoic acid] and the subsequent retro-aldol cleavage of the hydrated intermediate to yield vanillin (4-hydroxy-3-methoxy-benzaldehyde). The structure contains 12 molecules in the asymmetric unit, in which HCHL assumes a hexameric structure of two stacked trimers. The substrate, feruloyl-CoA, was modelled into the active site based on the structure of enoyl-CoA hydratase bound to the feruloyl-CoA-like substrate 4-(N,N-dimethylamino)-cinnamoyl-CoA (PDB code 1ey3). Feruloyl-CoA was bound in this model between helix 3 of the A subunit and helix 9 of the B subunit. A highly ordered structural water in the HCHL structure coincided with the thioester carbonyl of feruloyl-CoA in the model, suggesting that the oxyanion hole for stabilization of a thioester-derived enolate, characteristic of coenzyme-A dependent members of the crotonase superfamily, is conserved. The model also suggested that a strong hydrogen bond between the phenolic hydroxyl groups of feruloyl-CoA and BTyr239 may be an important determinant of the enzyme's ability to discriminate between the natural substrate and cinnamoyl-CoA, which is not a substrate.
The line below this paragraph, {{ABSTRACT_PUBMED_17139085}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17139085 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17139085}}


==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Vanillin]]
[[Category: Vanillin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:22:05 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:48:16 2008''

Revision as of 17:48, 27 July 2008

File:2j5i.png

Template:STRUCTURE 2j5i

CRYSTAL STRUCTURE OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASE

Template:ABSTRACT PUBMED 17139085

About this Structure

2J5I is a Protein complex structure of sequences from Pseudomonas fluorescens. Full crystallographic information is available from OCA.

Reference

The 1.8 A resolution structure of hydroxycinnamoyl-coenzyme A hydratase-lyase (HCHL) from Pseudomonas fluorescens, an enzyme that catalyses the transformation of feruloyl-coenzyme A to vanillin., Leonard PM, Brzozowski AM, Lebedev A, Marshall CM, Smith DJ, Verma CS, Walton NJ, Grogan G, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1494-501. Epub, 2006 Nov 23. PMID:17139085

Page seeded by OCA on Sun Jul 27 20:48:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA